| Summary: | 碩士 === 國立高雄海洋科技大學 === 水產食品科學研究所 === 99 === Protein hydrolysates from Achatina fulica foot muscle was extracted by high-temperature hydrolysis (121℃, 15-90 min) to obtain a retorted Achatina fulica protein hydrolysates (RAFPH). RAFPH obtained at 60 min was selected to further hydrolyzed with three enzymes (e.g. papain, tripsin, and alcalase) The RAFPH and enzymatic-treated RAFPH was analyzed for their degree of hydrolysis, molecular weight distribution, soluble protein, peptide content, antioxidant capacity, together with measurement of cholesterol-micelles disintegration , fat adsorption, emulsion capacity and foam capacity. The degree of hydrolysis of RAFPH obtained after 15−90 min hydrolysis reached about 74.4-78.0%. Using the gel filtration chromatography on a Superdex Peptide 10/300, the major molecule weight of protein hydrolysates was in the range of 686−6,511 Da. Soluble protein and peptide contents of the RAFPH were increased with prolonged hydrolysis time. For determination of In vitro disintegration of cholesterol in mixed micell, significant decreased concentrations of cholesterol-micelle was observed at high-temperature extraction as well as hydrolysis with papain, trypsin and alcalase, relative to control implying the ability to reduce cholesterol absorption. In the evaluation of physiochemical properties, fat absorption capacity, emulsifying capacity, foaming capacity of RAFPH obtained after hydrolysis for 15 min were better than the other, were as high as 2.27 g, 3.35 mL and 62.9%, respectively. The lower physicochemical properties of RAFPH digested with enzymatic hydrolysis relative to the RAFPH along is attributed to the excessive hydrolysis. This study revealed that all RAFPH was found to have a good antioxidant effect on 86.6-91.8% scavenging activity of DPPH radical, 94.1-98.2% inhibition ratio of linoleic acid oxidation, 95.9-97.0% trolox equivalent antioxidant capacity, and reducing power of 0.360-0.407 value (OD 700 nm). In addition, RAFPH treated with alcalase and papain had better antioxidant capacity than that trypsin treated RAFPH.
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